Deaminated glutathione amidase (NIT1)

The protein contains 327 amino acids for an estimated molecular weight of 35896 Da.

 

Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione. Plays a role in cell growth and apoptosis: loss of expression promotes cell growth, resistance to DNA damage stress and increased incidence to NMBA-induced tumors. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. (updated: Jan. 31, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 98%
Model score: 36

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The reference OMIM entry for this protein is 604618

Nitrilase 1; nit1

CLONING

Bacterial and plant nitrilases are enzymes that cleave nitriles and organic amides to the corresponding carboxylic acids plus ammonia. By searching an EST database with the sequence of the nitrilase domain of the Drosophila NitFhit protein, Pekarsky et al. (1998) identified human ESTs encoding nitrilase-1 (NIT1). They found that the NIT1 gene is expressed as alternatively spliced transcripts. The major NIT1 transcript encodes a deduced 327-amino acid protein that shares 90% amino acid sequence identity with mouse Nit1, 58% identity with the nitrilase domain of C. elegans NitFhit, and 53% identity with the nitrilase domain of Drosophila NitFhit. The NIT1 gene spans approximately 3.2 kb and contains 7 exons. Northern blot analysis detected NIT1 transcripts of approximately 1.4 and 2.4 kb in all adult tissues examined, namely heart, brain, lung, liver, pancreas, kidney, skeletal muscle, and placenta. An approximately 1.2-kb NIT1 transcript was found in skeletal muscle and heart.

MAPPING

By radiation hybrid mapping, Pekarsky et al. (1998) mapped the human NIT1 gene to chromosome 1q21-q22. They mapped the mouse Nit1 gene to distal chromosome 1, between the D1Mit35 and D1Mit209 markers. This region of mouse chromosome 1 shares homology of synteny with human 1q. ... More on the omim web site

Subscribe to this protein entry history

Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604618 was added.